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Int. J. Mol. Sci. 2016, 17(8), 1363; doi:10.3390/ijms17081363

Antimicrobial Protein Candidates from the Thermophilic Geobacillus sp. Strain ZGt-1: Production, Proteomics, and Bioinformatics Analysis

1
Biotechnology, Department of Chemistry, Lund University, Lund SE-221 00, Sweden
2
Center for Molecular Protein Science, Department of Chemistry, Lund University, Lund SE-221 00, Sweden
3
Department of Microbiology and Immunology, Faculty of Pharmacy, Beni-Suef University, Beni-Suef 62511, Egypt
4
Applied Microbiology, Department of Chemistry, Lund University, Lund SE-221 00, Sweden
5
Department of Biology, Microbial Ecology Group, Lund University, Lund SE-221 00, Sweden
*
Author to whom correspondence should be addressed.
Academic Editor: Már Másson
Received: 17 June 2016 / Revised: 1 August 2016 / Accepted: 12 August 2016 / Published: 19 August 2016
(This article belongs to the Special Issue Drug Delivery and Antimicrobial Agents)
View Full-Text   |   Download PDF [1802 KB, uploaded 23 August 2016]   |  

Abstract

A thermophilic bacterial strain, Geobacillus sp. ZGt-1, isolated from Zara hot spring in Jordan, was capable of inhibiting the growth of the thermophilic G. stearothermophilus and the mesophilic Bacillus subtilis and Salmonella typhimurium on a solid cultivation medium. Antibacterial activity was not observed when ZGt-1 was cultivated in a liquid medium; however, immobilization of the cells in agar beads that were subjected to sequential batch cultivation in the liquid medium at 60 °C showed increasing antibacterial activity up to 14 cycles. The antibacterial activity was lost on protease treatment of the culture supernatant. Concentration of the protein fraction by ammonium sulphate precipitation followed by denaturing polyacrylamide gel electrophoresis separation and analysis of the gel for antibacterial activity against G. stearothermophilus showed a distinct inhibition zone in 15–20 kDa range, suggesting that the active molecule(s) are resistant to denaturation by SDS. Mass spectrometric analysis of the protein bands around the active region resulted in identification of 22 proteins with molecular weight in the range of interest, three of which were new and are here proposed as potential antimicrobial protein candidates by in silico analysis of their amino acid sequences. Mass spectrometric analysis also indicated the presence of partial sequences of antimicrobial enzymes, amidase and dd-carboxypeptidase. View Full-Text
Keywords: thermophile; Geobacillus; antimicrobial proteins; SDS-resistant proteins; immobilization; cell-recycling; food spoilage bacteria thermophile; Geobacillus; antimicrobial proteins; SDS-resistant proteins; immobilization; cell-recycling; food spoilage bacteria
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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MDPI and ACS Style

Alkhalili, R.N.; Bernfur, K.; Dishisha, T.; Mamo, G.; Schelin, J.; Canbäck, B.; Emanuelsson, C.; Hatti-Kaul, R. Antimicrobial Protein Candidates from the Thermophilic Geobacillus sp. Strain ZGt-1: Production, Proteomics, and Bioinformatics Analysis. Int. J. Mol. Sci. 2016, 17, 1363.

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